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the in vivo effects were diametrically reversed with RIP3 (show RIPK3 Proteins) deletion or RIP1 (show UQCRFS1 Proteins) blockade, resulting in marked tumor protection. The dichotomy between the in vivo and in vitro results suggests that the microenvironmental milieu resulting from RIP1 (show UQCRFS1 Proteins)/RIP3 (show RIPK3 Proteins) signaling is likely responsible for its protumorigenic effects
Shikonin induces glioma cell necroptosis in vitro by reactive oxygen species overproduction and promoting RIP1 (show UQCRFS1 Proteins)/RIP3 (show RIPK3 Proteins) necrosome formation.
the cytoplasmic retinoic acid receptor gamma (show RARG Proteins) (RARgamma) controls receptor-interacting protein kinase (show CDK7 Proteins) 1 (RIP1 (show UQCRFS1 Proteins))-initiated cell death when cellular inhibitor of apoptosis (cIAP) activity is blocked.
SIRT2 (show SIRT2 Proteins) and RIPK1 were localized to the syncytiotrophoblast, villous leukocytes and vasculature in all preterm placentas. A significant reduction in SIRT2 (show SIRT2 Proteins) protein expression in both preeclampsia and fetal growth restricted placentas was identified. RIPK1 mRNA expression was significantly increased in preeclampsia placentas. Immunofluorescence identified both SIRT2 (show SIRT2 Proteins) and RIPK1 in the cytotrophoblast cytoplasm.
RIPK1 inhibits the transcriptional activity of VDR.
Results show that downregulation of RIP1 (show UQCRFS1 Proteins) results in increased resistance to SN38, implying a requirement for RIP1 (show UQCRFS1 Proteins) in mediating cytotoxicity through the TNF (show TNF Proteins)/TNFR (show TNFRSF1A Proteins) signaling pathway.
Renal clear cell carcinoma cells cells express increased amounts of RIPK1 and RIPK3 (show RIPK3 Proteins) and are poised to undergo necroptosis in response to TNFR1 (show TNFRSF1A Proteins) signaling.
Data suggest that pro-death signals through TIR-domain-containing adapter-inducing interferon-beta (show IFNB1 Proteins) (TRIF (show TRIM69 Proteins)) are regulated by autophagy and propose that pro-apoptotic signalling through TRIF (show TRIM69 Proteins)/RIPK1/caspase-8 (show CASP8 Proteins) occurs in fibrillary platforms.
UL45 promoted the UL48-RIP1 (show UQCRFS1 Proteins) interaction and re-localization of RIP1 (show UQCRFS1 Proteins) to the UL48-containing virion assembly complex.
we provide evidence that p62 (show GTF2H1 Proteins) is implicated in the activation of NF-kappaB (show NFKB1 Proteins) signaling that is partly dependent on RIP1 (show UQCRFS1 Proteins)
TNFalpha (show TNF Proteins)-induced phosphorylation of RIPK1 in the intermediate domain by TAK1 (show NR2C2 Proteins) plays a key role in regulating the decision between three distinct mechanisms of cell death: necroptosis, RIPK1-independent and dependent apoptosis.
K45 mediated kinase activity of RIPK1 is not only important for necroptosis but it also has a key role in promoting cytokine signaling and host response to inflammatory stimuli.
Data show that the kinase activity of receptor-interacting protein kinase (show CDK7 Proteins) 1 (RIPK1) is required for Yersinia-induced apoptosis.
p38MAPK (show MAPK14 Proteins)/MK2 (show KCNA2 Proteins) phosphorylation of RIPK1 is a crucial checkpoint for cell fate in inflammation and infection that determines the outcome of bacteria-host cell interaction.
MK2 (show KCNA2 Proteins)-mediated RIPK1 phosphorylation is an important molecular mechanism limiting the sensitivity of the cells to the cytotoxic effects of TNF (show TNF Proteins).
An alternative function for RIPK1/RIPK3 (show RIPK3 Proteins) in vascular permeability.
these results revealed a novel, kinase-independent function of RIP1, which is essential for not only promoting TCR-induced proliferative responses but also in blocking apoptosis in mature T cells.
Data show that the kinase domain of RIPK1 is a disease driver of intracerebral hemorrhage, mediating both acute cell death and functional outcome.
MK2 (show KCNA2 Proteins)-mediated phosphorylation of RIPK1 serves as a checkpoint within the TNF (show TNF Proteins) signaling pathway that integrates cell survival and cytokine production.
study identifies a novel role for RIPK1 and RIPK3 (show RIPK3 Proteins), a pair of homologous serine/threonine kinases previously implicated in the regulation of necroptosis and pathologic tissue injury, in directing IFN-beta (show IFNB1 Proteins) production in macrophagesges.
Serine-threonine kinase which transduces inflammatory and cell-death signals (necroptosis) following death receptors ligation, activation of pathogen recognition receptors (PRRs), and DNA damage. Upon activation of TNFR1 by the TNF-alpha family cytokines, TRADD and TRAF2 are recruited to the receptor. Ubiquitination by TRAF2 via 'Lys-63'-link chains acts as a critical enhancer of communication with downstream signal transducers in the mitogen-activated protein kinase pathway and the NF-kappa-B pathway, which in turn mediate downstream events including the activation of genes encoding inflammatory molecules. Polyubiquitinated protein binds to IKBKG/NEMO, the regulatory subunit of the IKK complex, a critical event for NF-kappa-B activation. Interaction with other cellular RHIM-containing adapters initiates gene activation and cell death. RIPK1 and RIPK3 association, in particular, forms a necroptosis-inducing complex.
receptor (TNFRSF)-interacting serine-threonine kinase 1
, 1,3,4,5,6-pentakisphosphate 2-kinase
, inositol polyphosphate kinase 1
, inositol-1,3,4,5,6-pentakisphosphate 2-kinase
, inositol-pentakisphosphate 2-kinase
, ins(1,3,4,5,6)P5 2-kinase
, insP5 2-kinase
, cell death protein RIP
, receptor interacting protein
, receptor-interacting protein 1
, receptor-interacting serine/threonine-protein kinase 1
, serine/threonine-protein kinase RIP
, RPA interacting protein delta 2
, RPA interacting protein epsilon
, RPA-interacting protein